1rl4: Difference between revisions

Revision as of 15:52, 21 February 2008

Plasmodium falciparum peptide deformylase complex with inhibitor

OverviewOverview

An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.

About this StructureAbout this Structure

1RL4 is a Single protein structure of sequence from Plasmodium falciparum 3d7 with , and as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Full crystallographic information is available from OCA.

ReferenceReference

An improved crystal form of Plasmodium falciparum peptide deformylase., Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG, Protein Sci. 2004 Apr;13(4):1155-63. Epub 2004 Mar 9. PMID:15010544

Page seeded by OCA on Thu Feb 21 14:52:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1rl4.jpg|left|200px]]<br /><applet load="1rl4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rl4.jpg|left|200px]]<br /><applet load="1rl4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rl4, resolution 2.18&Aring;" />
 '''Plasmodium falciparum peptide deformylase complex with inhibitor'''<br />
 ==Overview==
-An altered version of peptide deformylase from Plasmodium falciparum, (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has, submicromolar affinity for its target protein. The structure is solved at, 2.2 A resolution, an improvement over the 2.8 A resolution achieved during, the structural determination of unliganded PfPDF. This represents the, successful outcome of modifying the protein construct in order to overcome, adverse crystal contacts and other problems encountered in the study of, unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit, of the current structure. The active site of each monomer of PfPDF is, occupied by a proteolyzed fragment of the tripeptide-like inhibitor., Unexpectedly, each PfPDF subunit is associated with two nearly complete, molecules of the inhibitor, found at a protein-protein interface. This is, the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.
+An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.
 ==About this Structure==
-RL4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7] with CO, BRR and BL5 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RL4 OCA].
+RL4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7] with <scene name='pdbligand=CO:'>CO</scene>, <scene name='pdbligand=BRR:'>BRR</scene> and <scene name='pdbligand=BL5:'>BL5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RL4 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Hirsh, I.]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol, W G.J.]]
 [[Category: Kumar, A.]]
-[[Category: Nguyen, K.T.]]
+[[Category: Nguyen, K T.]]
 [[Category: Pei, D.]]
-[[Category: Robien, M.A.]]
+[[Category: Robien, M A.]]
 [[Category: Turley, S.]]
 [[Category: BL5]]
@@ Line 31: / Line 31: @@
 [[Category: plasmodium]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:52:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:03 2008''